ID   SP0A_CLOAB              Reviewed;         281 AA.
AC   P58253;
DT   29-AUG-2001, integrated into UniProtKB/Swiss-Prot.
DT   29-AUG-2001, sequence version 1.
DT   03-AUG-2022, entry version 125.
DE   RecName: Full=Stage 0 sporulation protein A homolog;
GN   Name=spo0A; OrderedLocusNames=CA_C2071;
OS   Clostridium acetobutylicum (strain ATCC 824 / DSM 792 / JCM 1419 / LMG 5710
OS   / VKM B-1787).
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=272562;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787;
RX   PubMed=11466286; DOI=10.1128/jb.183.16.4823-4838.2001;
RA   Noelling J., Breton G., Omelchenko M.V., Makarova K.S., Zeng Q., Gibson R.,
RA   Lee H.M., Dubois J., Qiu D., Hitti J., Wolf Y.I., Tatusov R.L., Sabathe F.,
RA   Doucette-Stamm L.A., Soucaille P., Daly M.J., Bennett G.N., Koonin E.V.,
RA   Smith D.R.;
RT   "Genome sequence and comparative analysis of the solvent-producing
RT   bacterium Clostridium acetobutylicum.";
RL   J. Bacteriol. 183:4823-4838(2001).
CC   -!- FUNCTION: May play the central regulatory role in sporulation. It may
CC       be an element of the effector pathway responsible for the activation of
CC       sporulation genes in response to nutritional stress. Spo0A may act in
CC       concert with spo0H (a sigma factor) to control the expression of some
CC       genes that are critical to the sporulation process (By similarity).
CC       {ECO:0000250}.
CC   -!- COFACTOR:
CC       Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250};
CC       Note=Binds 1 Ca(2+) ion per subunit. {ECO:0000250};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
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DR   EMBL; AE001437; AAK80030.1; -; Genomic_DNA.
DR   PIR; C97155; C97155.
DR   RefSeq; NP_348690.1; NC_003030.1.
DR   RefSeq; WP_010965371.1; NC_003030.1.
DR   AlphaFoldDB; P58253; -.
DR   SMR; P58253; -.
DR   STRING; 272562.CA_C2071; -.
DR   EnsemblBacteria; AAK80030; AAK80030; CA_C2071.
DR   GeneID; 44998553; -.
DR   KEGG; cac:CA_C2071; -.
DR   PATRIC; fig|272562.8.peg.2275; -.
DR   eggNOG; COG0745; Bacteria.
DR   HOGENOM; CLU_072509_0_0_9; -.
DR   OMA; TKELYPM; -.
DR   OrthoDB; 930905at2; -.
DR   Proteomes; UP000000814; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0003700; F:DNA-binding transcription factor activity; IEA:InterPro.
DR   GO; GO:0051606; P:detection of stimulus; IEA:InterPro.
DR   GO; GO:0000160; P:phosphorelay signal transduction system; IEA:UniProtKB-KW.
DR   GO; GO:0042173; P:regulation of sporulation resulting in formation of a cellular spore; IEA:InterPro.
DR   GO; GO:0030435; P:sporulation resulting in formation of a cellular spore; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.10.10; -; 1.
DR   InterPro; IPR011006; CheY-like_superfamily.
DR   InterPro; IPR016032; Sig_transdc_resp-reg_C-effctor.
DR   InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR   InterPro; IPR014879; Spo0A_C.
DR   InterPro; IPR012052; Spore_0_A.
DR   InterPro; IPR036388; WH-like_DNA-bd_sf.
DR   Pfam; PF00072; Response_reg; 1.
DR   Pfam; PF08769; Spo0A_C; 1.
DR   PIRSF; PIRSF002937; Res_reg_Spo0A; 1.
DR   SMART; SM00448; REC; 1.
DR   SUPFAM; SSF46894; SSF46894; 1.
DR   SUPFAM; SSF52172; SSF52172; 1.
DR   TIGRFAMs; TIGR02875; spore_0_A; 1.
DR   PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE   3: Inferred from homology;
KW   Activator; Calcium; Cytoplasm; DNA-binding; Metal-binding; Phosphoprotein;
KW   Reference proteome; Repressor; Sporulation; Transcription;
KW   Transcription regulation; Two-component regulatory system.
FT   CHAIN           1..281
FT                   /note="Stage 0 sporulation protein A homolog"
FT                   /id="PRO_0000081237"
FT   DOMAIN          7..125
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00169"
FT   DNA_BIND        213..232
FT                   /note="H-T-H motif"
FT                   /evidence="ECO:0000255"
FT   BINDING         12
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   BINDING         13
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   BINDING         58
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         58
FT                   /note="4-aspartylphosphate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00169"
SQ   SEQUENCE   281 AA;  31530 MW;  9D6A5DAF5482C4B3 CRC64;
     MESRKISVLI ADDNKEFCNI LNDYLLNQSD MIVVGIAKDG VEALKLIENK KPDLVVLDII
     MPRLDGLGVL EKLNNKDAEN LPRIIVLSAV GQDKITQRAI TLGADYYVVK PFDMDVFTNR
     IREMFNNTIS NSEQKRSYQV EEKEASFAGT IANDVYSDNI GNKAVDLESE ITSIIHQIGV
     PAHIKGYMYL REAITMVVNN MELLSAVTKE LYPSIAKKYN TTASRVERAI RHAIEVAWSR
     GQVETINKLF GYTINNGKGK PTNSEFIAMI ADKLRLKNKV S